LASP1
LIM and SH3 protein 1 | |||||||||||||
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File:PBB Protein LASP1 image.jpg PDB rendering based on 1zfo. | |||||||||||||
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Identifiers | |||||||||||||
Symbols | LASP1 ; Lasp-1; MLN50 | ||||||||||||
External IDs | Template:OMIM5 Template:MGI HomoloGene: 4480 | ||||||||||||
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RNA expression pattern | |||||||||||||
File:PBB GE LASP1 200618 at tn.png | |||||||||||||
More reference expression data | |||||||||||||
Orthologs | |||||||||||||
Template:GNF Ortholog box | |||||||||||||
Species | Human | Mouse | |||||||||||
Entrez | n/a | n/a | |||||||||||
Ensembl | n/a | n/a | |||||||||||
UniProt | n/a | n/a | |||||||||||
RefSeq (mRNA) | n/a | n/a | |||||||||||
RefSeq (protein) | n/a | n/a | |||||||||||
Location (UCSC) | n/a | n/a | |||||||||||
PubMed search | n/a | n/a |
LIM and SH3 protein 1, also known as LASP1, is a human gene.[1]
This gene encodes a member of a LIM protein subfamily which is characterized by a LIM motif and a domain of Src homology region 3. This protein functions as an actin-binding protein and possibly in cytoskeletal organization.[1]
References
Further reading
- Tomasetto C, Régnier C, Moog-Lutz C; et al. (1996). "Identification of four novel human genes amplified and overexpressed in breast carcinoma and localized to the q11-q21.3 region of chromosome 17". Genomics. 28 (3): 367–76. doi:10.1006/geno.1995.1163. PMID 7490069.
- Tomasetto C, Moog-Lutz C, Régnier CH; et al. (1995). "Lasp-1 (MLN 50) defines a new LIM protein subfamily characterized by the association of LIM and SH3 domains". FEBS Lett. 373 (3): 245–9. PMID 7589475.
- Chew CS, Parente JA, Zhou C; et al. (1998). "Lasp-1 is a regulated phosphoprotein within the cAMP signaling pathway in the gastric parietal cell". Am. J. Physiol. 275 (1 Pt 1): C56–67. PMID 9688835.
- Schreiber V, Moog-Lutz C, Régnier CH; et al. (1999). "Lasp-1, a novel type of actin-binding protein accumulating in cell membrane extensions". Mol. Med. 4 (10): 675–87. PMID 9848085.
- Chew CS, Chen X, Parente JA; et al. (2003). "Lasp-1 binds to non-muscle F-actin in vitro and is localized within multiple sites of dynamic actin assembly in vivo". J. Cell. Sci. 115 (Pt 24): 4787–99. PMID 12432067.
- Strausberg RL, Feingold EA, Grouse LH; et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.
- Butt E, Gambaryan S, Göttfert N; et al. (2003). "Actin binding of human LIM and SH3 protein is regulated by cGMP- and cAMP-dependent protein kinase phosphorylation on serine 146". J. Biol. Chem. 278 (18): 15601–7. doi:10.1074/jbc.M209009200. PMID 12571245.
- Gevaert K, Goethals M, Martens L; et al. (2004). "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides". Nat. Biotechnol. 21 (5): 566–9. doi:10.1038/nbt810. PMID 12665801.
- Ota T, Suzuki Y, Nishikawa T; et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
- Li B, Zhuang L, Trueb B (2004). "Zyxin interacts with the SH3 domains of the cytoskeletal proteins LIM-nebulette and Lasp-1". J. Biol. Chem. 279 (19): 20401–10. doi:10.1074/jbc.M310304200. PMID 15004028.
- Keicher C, Gambaryan S, Schulze E; et al. (2004). "Phosphorylation of mouse LASP-1 on threonine 156 by cAMP- and cGMP-dependent protein kinase". Biochem. Biophys. Res. Commun. 324 (1): 308–16. doi:10.1016/j.bbrc.2004.08.235. PMID 15465019.
- Gerhard DS, Wagner L, Feingold EA; et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMID 15489334.
- Tao WA, Wollscheid B, O'Brien R; et al. (2005). "Quantitative phosphoproteome analysis using a dendrimer conjugation chemistry and tandem mass spectrometry". Nat. Methods. 2 (8): 591–8. doi:10.1038/nmeth776. PMID 16094384.
- Rual JF, Venkatesan K, Hao T; et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
- Grunewald TG, Kammerer U, Schulze E; et al. (2006). "Silencing of LASP-1 influences zyxin localization, inhibits proliferation and reduces migration in breast cancer cells". Exp. Cell Res. 312 (7): 974–82. doi:10.1016/j.yexcr.2005.12.016. PMID 16430883.
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